ReviewCold Spring Harbor perspectives in biology2016
Yeast and Fungal Prions.
Review in Cold Spring Harbor perspectives in biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
54 citing papers in PubMed, 85 citations in OpenAlex.
- Role of Microbial Toxins in Neurodegenerative Diseases: Insights and Future Perspectives.Biomolecules · 2026Review
- Transcriptomic analysis of Rnq1 loss and prionization reveals alterations in translation pathways and energy metabolism.Scientific reports · 2026Article
- The Importance of Being Imperfect: Structure and Function of Bacterial Amyloid.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Review
- Massive experimental quantification allows interpretable deep learning of protein aggregation.Science advances · 2025Article
- Osmotic stress induces formation of both liquid condensates and amyloids by a yeast prion domain.The Journal of biological chemistry · 2024Article
- Massive experimental quantification of amyloid nucleation allows interpretable deep learning of protein aggregation.bioRxiv : the preprint server for biology · 2024Article
- Mrj is a chaperone of the Hsp40 family that regulates Orb2 oligomerization and long-term memory in Drosophila.PLoS biology · 2024Article
- Multiple aspects of amyloid dynamicsFrontiers in molecular neuroscience · 2024Article
- Emergence of the fungal immune system.iScience · 2023Review
- Methionine Sulfoxide Reductases Suppress the Formation of the [Antioxidants (Basel, Switzerland) · 2023Article
- Cellular Prion Protein Role in Cancer Biology: Is It A Potential Therapeutic Target?Biomedicines · 2022Review
- The Mutability of Yeast Prions.Viruses · 2022Article
- Amyloid Fragmentation and Disaggregation in Yeast and Animals.Biomolecules · 2021Review
- Yeast J-protein Sis1 prevents prion toxicity by moderating depletion of prion protein.Genetics · 2021Article
- Article
- MicroRNAs in Prion Diseases-From Molecular Mechanisms to Insights in Translational Medicine.Cells · 2021Review
- Effect of spin labelling on the aggregation kinetics of yeast prion protein Ure2.Royal Society open science · 2021Article
- Unbelievable but True: Epigenetics and Chromatin in Fungi.Trends in genetics : TIG · 2021Review
- Structures of Pathological and Functional Amyloids and Prions, a Solid-State NMR Perspective.Frontiers in molecular neuroscience · 2021Review
- Possible Role of Activin in the Adiponectin Paradox-Induced Progress of Alzheimer's Disease.Journal of Alzheimer's disease : JAD · 2021Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
1 author at 1 institution in 1 country.
Funding
Abstract
Yeast and fungal prions are infectious proteins, most being self-propagating amyloids of normally soluble proteins. Their effects range from a very mild detriment to lethal, with specific effects dependent on the prion protein and the specific prion variant ("prion strain"). The prion amyloids of Sup35p, Ure2p, and Rnq1p are in-register, parallel, folded β-sheets, an architecture that naturally suggests a mechanism by which a protein can template its conformation, just as DNA or RNA templates its sequence. Prion propagation is critically affected by an array of chaperone systems, most notably the Hsp104/Hsp70/Hsp40 combination, which is responsible for generating new prion seeds from old filaments. The Btn2/Cur1 antiprion system cures most [URE3] prions that develop, and the Ssb antiprion system blocks [PSI+] generation.
Indexed as
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What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.